ArticlePlant signaling & behavior2018
Autophosphorylation site Y428 is essential for the in vivo activation of CERK1.
Article in Plant signaling & behavior, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 25 citations in OpenAlex.
- The receptor MIK2 interacts with the kinase RKS1 to control quantitative disease resistance to Xanthomonas campestris.Plant physiology · 2024Article
- Review
- The Arabidopsis E3 ubiquitin ligase PUB4 regulates BIK1 and is targeted by a bacterial type-III effector.The EMBO journal · 2022Article
- Activation loop phosphorylation of a non-RD receptor kinase initiates plant innate immune signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Importance of tyrosine phosphorylation for transmembrane signaling in plants.The Biochemical journal · 2021Review
- Cytoplasmic interaction of LysM receptors contributes to the formation of symbiotic receptor complex.Plant biotechnology (Tokyo, Japan) · 2020Article
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5 authors at 1 institution in 1 country.
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Abstract
Autophosphorylation of PRR is a critical event for the activation of immune signaling in plant. However, the detailed function of these phosphorylation sites is still not well understood. We analyzed the function of an autophosphorylation site of Arabidopsis CERK1, Y428, in immune signaling. Biochemical characterization of CERK1 mutants transiently expressed in N. benthamiana indicated that Y428 plays a crucial role for the in vivo activation of CERK1, differently from the previous observation by the in vitro kinase assay with its cytoplasmic domain. Similar discrepancy between in vitro and in vivo kinase assay was also reported for the corresponding phosphorylation site of EFR, suggesting that these conserved tyrosine residues play important roles for the activation of both RD and non-RD RLKs.
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